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Association of bovine αs1- and β-casein using the fluorescent properties of 1,8-anilinonaphthalene sulphonate

Published online by Cambridge University Press:  01 June 2009

L. K. Creamer  and
J. V. Wheelock
L. K. Creamer
Affiliation:
New Zealand Dairy Research Institute, Palmerston North, New Zealand
J. V. Wheelock
Affiliation:
School of Biological Sciences, University of Bradford, Bradford, England
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Summary

The effects of NaCl, CaCl2 and temperature on the emitted fluorescence of anilinonaphthalene sulphonate (ANS) in solutions of αs1- and β-casein indicated that the ANS was associated with the protein. Increased aggregation of the protein was responsible for further enhancement of the fluorescence. Addition of CaCl2 to a mixture of αs1- and β-casein at 37 °C caused a greater increase in fluorescence than when αs1- or β-casein was used alone, supporting the suggestion that these 2 proteins form co-polymers with different properties from the homopolymers and indicating that hydrophobic bonding between αs1- and β-casein may be important in the presence of Ca.

Type
Research Article
Information
Journal of Dairy Research , Volume 42 , Issue 3 , October 1975 , pp. 381 - 389
Copyright
Copyright © Proprietors of Journal of Dairy Research 1975

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